Kallikrein

Names

[ Name ]:
Kallikrein

[Synonym ]:
MFCD00131428
5-(Ethoxycarbonyl)-4-(2-ethoxy-2-oxoethyl)-2-methyl-1H-pyrrole-3-carboxylic acid
1H-Pyrrole-2,4-dicarboxylic acid, 3-(2-ethoxy-2-oxoethyl)-5-methyl-, 2-ethyl ester
kallidinogenase

Biological Activity

[Description]:

Kallikrein is capable of forming the kallikrenase kalinin system (KKS) in plasma and tissues, producing bradykinin and kalin peptides, respectively[1].

[Related Catalog]:

Research Areas >> Others

[References]

[1]. Campbell DJ, et al. The kallikrein-kinin system in humans. Clin Exp Pharmacol Physiol. 2001 Dec;28(12):1060-5.

Chemical & Physical Properties

[ Density]:
1.3±0.1 g/cm3

[ Boiling Point ]:
471.1±45.0 °C at 760 mmHg

[ Molecular Formula ]:
C₁₃H₁₇NO₆

[ Molecular Weight ]:
283.277

[ Flash Point ]:
238.7±28.7 °C

[ Exact Mass ]:
283.105591

[ LogP ]:
2.10

[ Appearance of Characters ]:
lyophilized powder

[ Vapour Pressure ]:
0.0±1.2 mmHg at 25°C

[ Index of Refraction ]:
1.543

[ Storage condition ]:
2-8°C

Safety Information

[ Personal Protective Equipment ]:
Eyeshields;Gloves;half-mask respirator (US);multi-purpose combination respirator cartridge (US)

[ Hazard Codes ]:
B

[ RIDADR ]:
NONH for all modes of transport

[ WGK Germany ]:
3

[ RTECS ]:
NZ2017050

Articles

BMPR2 is required for postimplantation uterine function and pregnancy maintenance.

J. Clin. Invest. 123(6) , 2539-50, (2013)

Abnormalities in cell-cell communication and growth factor signaling pathways can lead to defects in maternal-fetal interactions during pregnancy, including immunologic rejection of the fetal/placenta...

The structure of human microplasmin in complex with textilinin-1, an aprotinin-like inhibitor from the Australian brown snake.

PLoS ONE 8(1) , e54104, (2013)

Textilinin-1 is a Kunitz-type serine protease inhibitor from Australian brown snake venom. Its ability to potently and specifically inhibit human plasmin (K(i) = 0.44 nM) makes it a potential therapeu...

Neutron and X-ray crystallographic analysis of Achromobacter protease I at pD 8.0: protonation states and hydration structure in the free-form.

Biochim. Biophys. Acta 1834(8) , 1642-7, (2013)

The structure of the free-form of Achromobacter protease I (API) at pD 8.0 was refined by simultaneous use of single crystal X-ray and neutron diffraction data sets to investigate the protonation stat...

Related Compounds

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